Homology modeling and identification of serine 160 as nucleophile of the active site in a thermostable carboxylesterase from the archaeon Archaeoglobus fulgidus

Autor: Giuseppe Manco, G. Adamo, L. Camardella, V. Carratore, Ferdinando Febbraio, M. Rossi

Publikováno v: Scopus-Elsevier
Protein engineering
13 (2000): 197–200.
info:cnr-pdr/source/autori:Manco G, Camardella L, Febbraio F, Adamo G, Carratore V, Rossi M./titolo:Homology modeling and identification of serine 160 as nucleophile of the active site in a thermostable carboxylesterase from the archaeon Archaeoglobus fulgidus./doi:/rivista:Protein engineering (Print)/anno:2000/pagina_da:197/pagina_a:200/intervallo_pagine:197–200/volume:13

The hyperthermophilic Archaeon Archaeoglobus fulgidus has a gene (AF1763) which encodes a thermostable carboxylesterase belonging to the hormone-sensitive lipase (HSL)-like group of the esterase/lipase family. Based on secondary structure predictions

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f4afdf89d955722b74207637e9736e7
https://doi.org/10.1093/protein/13.3.197

Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B

Autor: L. Camardella, V. Carratore, G Damonte, U Benatti, A De Flora, Maria Antonietta Ciardiello

Publikováno v: Blood. 85:264-267

Human erythrocytes contain a nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein, FX, whose levels are significantly increased in erythrocytes from glucose-6-phosphate dehydrogenase (G6PD)- deficient individuals bearing the mediterr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4447f53b75ebdc7236ea80416c832980
https://doi.org/10.1182/blood.v85.1.264.bloodjournal851264

IS THE THE PARP-LIKE ENZYME FROM S. solfataricus STRUCTURALLY RELATED TO THE EUKARYOTIC COUNTERPARTS?

Autor: FARAONE MENNELLA, MARIA ROSARIA, S. CASTELLANO, V. CARRATORE, A. GAMBACORTA, B. NICOLAUS, FARINA, BENEDETTA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::8da258d4ed5fb3b1c7b95e35049ce4a3
http://hdl.handle.net/11588/185153

Hagfish hemoglobins. Structure, function and oxygen-linked association

Autor: A, Fago, L, Giangiacomo, R, D'Avino, V, Carratore, M, Romano, A, Boffi, E, Chiancone

Publikováno v: Journal of biological chemistry (Online) 276 (2001): 27415–27423.
info:cnr-pdr/source/autori:Fago A.1, Giangiacomo L.2, D'Avino R.3, Carratore V.3, Romano M.3, Boffi A.2, Chiancone E.2/titolo:Hagfish hemoglobins. Structure, function and oxygen-linked association/doi:/rivista:Journal of biological chemistry (Online)/anno:2001/pagina_da:27415/pagina_a:27423/intervallo_pagine:27415–27423/volume:276

Cyclostomes, hagfishes and lampreys, contain hemoglobins that are monomeric when oxygenated and polymerize to dimers or tetramers when deoxygenated. The three major hemoglobin components (HbI, HbII, and HbIII) from the hagfish Myxine glutinosa have b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::54aa0e929874f5637d0a4ed31044bf6b
https://publications.cnr.it/doc/8591

The hemoglobins of the antarctic fishes Atedidraco orianae and Pogonophryne scotti. Amino acid sequence, lack of cooperativity, and ligand binding properties

Autor: M, Tamburrini, M, Romano, V, Carratore, A, Kunzmann, M, Coletta, G, di Prisco

Publikováno v: The Journal of biological chemistry. 273(49)

The oxygen-transport system of two species of Antarctic fishes belonging to the family Artedidraconidae, Artedidraco orianae and Pogonophryne scotti, was thoroughly investigated. The complete amino acid sequence of the alpha and beta chains of the si

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6a233fb5928e24f3d25bc1b271d2d2dc
https://pubmed.ncbi.nlm.nih.gov/9829976